◀ Back to MAPK14
MAPK14 — TAB1
Pathways - manually collected, often from reviews:
-
KEGG NOD-like receptor signaling pathway:
Complex of MAP3K7-TAB1-TAB2-TAB3
→
MAPK11/MAPK12/MAPK13/MAPK14
(protein-protein, activation)
-
NCI Pathway Database Regulation of p38-alpha and p38-beta:
TAB1 (TAB1)
→
PGK/cGMP/p38 alpha complex (PRKG1-MAPK14)
(modification, collaborate)
Ge et al., Science 2002*, Cheung et al., EMBO J 2003, Lu et al., J Biol Chem 2006*, Kang et al., J Biol Chem 2006*, Fiedler et al., J Biol Chem 2006*
Evidence: mutant phenotype, assay, physical interaction, other species
-
NCI Pathway Database Regulation of p38-alpha and p38-beta:
TAB1 (TAB1)
→
p38 alpha (MAPK14)
(modification, collaborate)
Ge et al., Science 2002*, Cheung et al., EMBO J 2003, Lu et al., J Biol Chem 2006*, Kang et al., J Biol Chem 2006*, Fiedler et al., J Biol Chem 2006*
Evidence: mutant phenotype, assay, physical interaction, other species
-
NCI Pathway Database Regulation of p38-alpha and p38-beta:
TAB1 (TAB1)
→
p38 alpha/TAB1 complex (MAPK14-TAB1)
(modification, collaborate)
Ge et al., Science 2002*, Cheung et al., EMBO J 2003, Lu et al., J Biol Chem 2006*, Kang et al., J Biol Chem 2006*, Fiedler et al., J Biol Chem 2006*
Evidence: mutant phenotype, assay, physical interaction, other species
-
NCI Pathway Database Regulation of p38-alpha and p38-beta:
PGK/cGMP/p38 alpha complex (PRKG1-MAPK14)
→
p38 alpha/TAB1 complex (MAPK14-TAB1)
(modification, collaborate)
Ge et al., Science 2002*, Cheung et al., EMBO J 2003, Lu et al., J Biol Chem 2006*, Kang et al., J Biol Chem 2006*, Fiedler et al., J Biol Chem 2006*
Evidence: mutant phenotype, assay, physical interaction, other species
-
NCI Pathway Database Regulation of p38-alpha and p38-beta:
PGK/cGMP complex (PRKG1)
→
p38 alpha/TAB1 complex (MAPK14-TAB1)
(modification, collaborate)
Ge et al., Science 2002*, Cheung et al., EMBO J 2003, Lu et al., J Biol Chem 2006*, Kang et al., J Biol Chem 2006*, Fiedler et al., J Biol Chem 2006*
Evidence: mutant phenotype, assay, physical interaction, other species
-
NCI Pathway Database Regulation of p38-alpha and p38-beta:
p38 alpha (MAPK14)
→
p38 alpha/TAB1 complex (MAPK14-TAB1)
(modification, collaborate)
Ge et al., Science 2002*, Cheung et al., EMBO J 2003, Lu et al., J Biol Chem 2006*, Kang et al., J Biol Chem 2006*, Fiedler et al., J Biol Chem 2006*
Evidence: mutant phenotype, assay, physical interaction, other species
-
NCI Pathway Database p38 MAPK signaling pathway:
TAB family (TAB2/TAB1)
→
p38alpha-beta-active (MAPK14/MAPK11)
(modification, collaborate)
Wang et al., Nature 2001, Cheung et al., EMBO J 2003, Shibuya et al., Science 1996
Evidence: mutant phenotype, physical interaction
-
NCI Pathway Database p38 MAPK signaling pathway:
p38alpha-beta-active (MAPK14/MAPK11)
→
TAK1/TAB family complex (MAP3K7-TAB2_TAB1)
(modification, inhibits)
Wang et al., Nature 2001, Cheung et al., EMBO J 2003, Shibuya et al., Science 1996
Evidence: mutant phenotype, physical interaction
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
-
IRef Bind_translation Interaction:
TAB1
—
MAPK14
(coimmunoprecipitation)
Tanno et al., Circ Res 2003*
-
IRef Biogrid Interaction:
TAB1
—
MAPK14
(physical association, affinity chromatography technology)
Ge et al., Science 2002*
-
IRef Biogrid Interaction:
TAB1
—
MAPK14
(direct interaction, two hybrid)
Vinayagam et al., Science signaling 2011
-
IRef Biogrid Interaction:
TAB1
—
MAPK14
(physical association, affinity chromatography technology)
Ge et al., J Biol Chem 2003*
-
IRef Biogrid Interaction:
TAB1
—
MAPK14
(direct interaction, pull down)
Ge et al., Science 2002*
-
IRef Hprd Interaction:
MAPK14
—
TAB1
(in vitro)
Ge et al., Science 2002*
-
IRef Hprd Interaction:
Complex of MAPK14-TAB1-MAPK14-TRAF6-TRAF6-TRAF6-TAB1-MAPK14-TAB1
(in vivo)
Ge et al., Science 2002*
-
IRef Intact Interaction:
TAB1
—
MAPK14
(physical association, coimmunoprecipitation)
Ge et al., Science 2002*
-
IRef Intact Interaction:
TAB1
—
MAPK14
(physical association, two hybrid)
Ge et al., Science 2002*
-
IRef Intact Interaction:
TAB1
—
MAPK14
(physical association, two hybrid)
Vinayagam et al., Science signaling 2011
-
IRef Ophid Interaction:
TAB1
—
MAPK14
(aggregation, confirmational text mining)
Ge et al., Science 2002*
-
IRef Ophid Interaction:
TAB1
—
MAPK14
(aggregation, interologs mapping)
Brown et al., Bioinformatics 2005
Text-mined interactions from Literome
McDermott et al., J Biol Chem 2002
:
In addition we found a
role for
TAK-1 in the activation of p38
MAPK by IL-1, with TAK-1 also associating with active Ras
Cheung et al., EMBO J 2003
:
Our results suggest that TAB1 participates in a
SAPK2a/p38alpha mediated feedback control of
TAK1 , which not only limits the activation of SAPK2a/p38alpha but synchronizes its activity with other signalling pathways that lie downstream of TAK1 ( JNK and IKK )
Cheung et al., Biochem J 2004
:
The SAPK2a/p38alpha mediated phosphorylation of TAB2 and TAB3 may contribute to the
SAPK2a/p38alpha mediated feedback control of
TAK1 activity that also involves the phosphorylation of TAB1
Singhirunnusorn et al., J Biol Chem 2005
:
Furthermore, SB203580 and p38alpha small interfering RNA enhanced TNF-alpha induced Thr-187 phosphorylation as well as TAK1 kinase activity, indicating that the phosphorylation is affected by
p38alpha/TAB1/TAB2 mediated feedback control of
TAK1
Makeeva et al., International journal of biological sciences 2007
:
The aim of present study was to elucidate the
role of
TAB1 in nitric oxide induced activation of p38
MAPK
Kim et al., American journal of physiology. Renal physiology 2007
:
TGF-beta activated kinase 1 and
TAK1 binding protein 1 cooperate to
mediate TGF-beta1 induced MKK3-p38
MAPK activation and stimulation of type I collagen
Windheim et al., Biochem J 2007
:
We also show that RIP2
induces the activation of the protein kinase
TAK1 ( transforming-growth-factor-beta activated kinase-1 ), that a dominant negative mutant of TAK1 inhibits RIP2 induced activation of JNK ( c-Jun N-terminal kinase ) and p38alpha
MAPK , and that signalling downstream of NOD2 or RIP2 is reduced by the TAK1 inhibitor ( 5Z ) -7-oxozeaenol or in TAK1-deficient cells
Makeeva et al., Endocrinology 2008
:
Transforming growth factor-beta activated protein kinase 1-binding protein (
TAB)-1alpha , but not TAB1beta,
mediates cytokine induced p38
mitogen activated protein kinase phosphorylation and cell death in insulin producing cells ... Transforming growth factor-beta activated protein kinase 1-binding protein ( TAB)-1alpha, but not
TAB1beta ,
mediates cytokine induced p38
mitogen activated protein kinase phosphorylation and cell death in insulin producing cells
Mendoza et al., Biochem J 2008
:
Studies using TAB1 ( -/- ) MEFs indicate important
roles for
TAB1 in recruiting p38alpha
MAPK to the TAK1 complex for the phosphorylation of TAB3 at Ser ( 60 ) and Thr ( 404 ) and in inhibiting the dephosphorylation of TAB3 at Ser ( 506 )
Kodym et al., RNA 2008
(MAP Kinase Signaling System) :
Activation of
TAK1-D leads to the downstream activation of the p38
MAPK and of SAPK/JNK but not the NFkappaB pathway
Mikkelsen et al., J Biol Chem 2009
:
We also observed that TRAF2 and
TAK1 were
essential for RIG-I mediated activation of p38
MAPK
Cheng et al., J Biomed Mater Res A 2010
(Inflammation...) :
The critical
role for
TAK1 in
p38MAPK and NFkappaB activation was as well confirmed by the inhibition of p38MAPK and NFkappaB activity following 5Z-7-oxozeaenol, a selective inhibitor of TAK1
Wolf et al., PloS one 2011
:
The TAB1 mutant lacking aa 452-457 decreases
TAB1 dependent phosphorylation of p38
MAPK
Tran et al., J Biol Chem 2012
(MAP Kinase Signaling System) :
In agreement with this, overexpression of ASK1 or
TAK1 resulted in enhanced
p38MAPK activation, and their knockdown inhibited p38MAPK in C2C12 cells
Yumoto et al., J Biol Chem 2013
(Cleft Palate) :
Our studies show that in neural crest derived craniofacial ecto-mesenchymal cells,
Tak1 is not only
required for TGF-ß- and bone morphogenetic protein induced p38
Mapk activation but also plays a role in agonist induced C-terminal and linker region phosphorylation of the receptor mediated R-Smads